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FLASH GENE
Symbol FKBP10 contributors: mct/npt - updated : 06-03-2017
HGNC name FK506 binding protein 10, 65 kDa
HGNC id 18169
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
10 - 2888 64 582 - 2002 12036304
EXPRESSION
Type restricted
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Skeletonappendicular skeleton   highly Homo sapiens
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Connectivebone    Homo sapiensAdult
Connectivedensetendon   Homo sapiensAdult
Connectivedenseligament   Homo sapiensAdult
cell lineage
cell lines
fluid/secretion
at STAGE
physiological period embryo, fetal
Text developing lung, vascular and airway smooth muscle cells
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • four N terminal FK506 binding
  • peptidyl prolyl cis-trans isomerase (ratamase) domains
  • three tetratricopeptide repeat (TPR) motifs consistent with nuclear transcript or chaperone activity
  • mono polymer monomer
    HOMOLOGY
    Homologene
    FAMILY
  • immunophilin class of proteins family
  • CATEGORY chaperone/stress , enzyme , tumor suppressor , transport
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,lumen
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    text colocalizing with tropoelastin in E.R dissociating before the Golgi apparatus
    basic FUNCTION
  • having a peptidylprolyl cis-trans-isomerase activity
  • able to interact with triple helical collagen, and acts as a collagen chaperone
  • may act as an elastin chaperone by controlling both the coacervation and the maturation stages of its self-assembly into fibrils
  • tumor suppressor function of the FKBP65 protein in ovarian carcinogenesis
  • is likely required for lysyl hydroxylase activity or access to type I collagen telopeptide lysines, perhaps through its function as a peptidylprolyl isomerase
  • FKBP10, PLOD2 and SERPINH1, acts during procollagen maturation to contribute to molecular stability and post-translational modification of type I procollagen, without which bone mass and quality are abnormal and fractures and contractures result
  • ability of FKBP10 to modulate the self-assembly of tropoelastin (ELN) is independent of its enzymatic activity to promote the cis-trans isomerization of proline residues in proteins
  • requirement for FKBP10 function during embryonic connective tissue development in mice, but the restricted expression postnatally in bone, ligaments and tendons correlates with the bone fragility and contracture phenotype in humans
  • SERPINH1 and FKBP10 act cooperatively during posttranslational maturation of type I procollagen but fail to properly interact in mutant SERPINH1 cells
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS development , cellular trafficking transport
    text organogenesis
    PATHWAY
    metabolism
    signaling
    a component
  • FKBP10 forms complexes with PLOD2 splice variants LH2A and LH2B but not with PLOD1 and PLOD3
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • ability of FKBP10 to modulate the self-assembly of ELN is independent of its enzymatic activity to promote the cis-trans isomerization of proline residues in proteins
  • FKBP10 is linked to pyridinoline cross-linking by specifically mediating the dimerization of PLOD2
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s) OIDP , BRKS1
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral     --low  
    in epithelial ovarian cancer cells compared to benign tumor cells and to ovarian epithelium
    constitutional     --low  
    altered collagen crosslinking through FKBP10 ablation in osteoblasts primarily leads to a qualitative defect in the skeleton
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
  • in Fkbp10 knockout mice, collagen telopeptide hydroxylysine crosslinking is dramatically reduced
  • Fkbp10(-/-) mouse embryonic fibroblasts show retention of procollagen in the cell layer and associated dilated endoplasmic reticulum